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Binding of FKBP23 to BiP in ER Shown by Gel Filtration Chromatography

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Binding of FKBP23 to BiP in ER Shown by Gel Filtration Chromatography

Chen Chen

a

, Hui Ma

a

, Ying Wang

a

, and Huaifeng Mi

a,b,

*

a Biochemical Section of Key Laboratory of Functional Polymer Materials,

Ministry of Education of China, Institute of Polymer Chemistry, Nankai University, 300071 Tianjin, China. Fax: (+86) 22 23 50 27 49. E-mail: hfmi@nankai.edu.cn

b Medical School of Nankai University, 300071 Tianjin, China

* Author for correspondence and reprint requests

Z. Naturforsch.62 c, 133Ð137 (2007); received July 24/August 31, 2006

FKBP23 was found in mouse endoplasmic reticulum (ER) in 1998. It consists of an N-terminal peptidyl-prolyl cis/trans isomerase (PPIase) domain and a C-terminal domain with Ca2+binding sites. Previously, we reported that FKBP23 specifically binds to BiP, the main protein of the molecular chaperone Hsp70 in ER lumen, and the binding is interrelated with the Ca2+ concentration. In this work we have found the existence of the complex FKBP23/BiP by separation of an ER extract using gel filtration chromatography (GFC), and that the existence of this complex is Ca2+-interrelated. This result further verified the Ca2+- interrelated binding of these two proteinsin vivo.

Key words:FKBP23, BiP, Gel Filtration Chromatography

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